Séminaire Harm H. Kampinga– 15 Avril 2026

Dr. Harm H. Kampinga

Dept. Biomedical Sciences, UMCG/RuG, Groningen, The Netherlands

Invité par Dr. Valérie Mezger

“Collapse of protein homeostasis as driver of age-related protein aggregation diseases“

Le séminaire se tiendra à l’Institut Jacques Monod, salle François Jacob (RB-18B). Bâtiment Buffon,

15 rue Hélène Brion, Paris 13.

Le mercredi 15 avril 2026 à 11h.

Publications de l’intervenant :

• Wentink et al., Mechanisms and regulation of the Hsp70 chaperone network. Nat Rev Mol Cell Biol. 2026, 27(2):110-128
• Mauthe et al., A chaperone-proteasome-based fragmentation machinery is essential for aggrephagy. Nat Cell Biol. 2025, 27(9):1448-1464
• Korsten et al., Nuclear poly-glutamine aggregates rupture the nuclear envelope and hinder its repair. J Cell Biol. 2024; 223(11):e202307142.
• Kuiper et al., The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis. Nat Cell Biol. 2022, 24(11):1584-1594
• Huiting et al., Targeting DNA topoisomerases or checkpoint kinases results in an overload of chaperone systems, triggering aggregation of a metastable subproteome. 2022, 11:e70726.
• Thiruvalluvan et al., DNAJB6, a Key Factor in Neuronal Sensitivity to Amyloidogenesis. Mol Cell. 2020,78(2):346-358.
• Kakkar V et al., The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model. Mol Cell. 2016, 62(2):272-283.
• Vos et al., Specific protein homeostatic functions of small heat-shock proteins increase lifespan. Aging Cell. 2016, 15(2):217-226.
• Vos et al., HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones. Hum Mol Genet. 2010, 19(23):4677-4693.
• Hageman et al., A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation. Mol Cell. 2010, 37(3):355-69.